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Crystal structure and biochemical characterization of malate dehydrogenase from Metallosphaera sedula.

Abstract：

:Metallosphaera sedula is a thermoacidophilic autotrophic archaeon and known to utilize the 3-hydroxypropionate/4-hydroxybutyrate cycle (3-HP/4-HB cycle) as a carbon fixation pathway. The 3-HP/4-HB cycle in M. sedula is associated with central metabolism, and malate dehydrogenase (MDH) is an enzyme involved in the central metabolism that converts malate to oxaloacetate. To elucidate the enzymatic properties of MDH from M. sedula (MsMDH), we determined the crystal structure of MsMDH as a complex with NAD+ and a ternary complex with malate and NAD+. Based on its complex structures and biochemical experiments, we observed that MsMDH can utilize both NAD+ and NADP+ as a cofactor. In addition, we revealed that MsMDH shows a conformational change at the active site upon substrate binding. Based on the comparison with other MDHs, we revealed that MsMDH was distinguished from general MDHs due to a Lys80 residue, and this difference is likely to influence the unique cofactor specificity of MsMDH.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Lee D,Hong J,Kim KJ

doi

10.1016/j.bbrc.2019.01.018

subject

Has Abstract

pub_date

2019-02-12 00:00:00

pages

833-838

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(19)30024-5

journal_volume

509

pub_type

杂志文章

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